ID PUR7_ALCBS Reviewed; 238 AA. AC Q0VRH1; DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot. DT 05-SEP-2006, sequence version 1. DT 16-JUN-2009, entry version 23. DE RecName: Full=Phosphoribosylaminoimidazole-succinocarboxamide synthase; DE EC=6.3.2.6; DE AltName: Full=SAICAR synthetase; GN Name=purC; OrderedLocusNames=ABO_0779; OS Alcanivorax borkumensis (strain SK2 / ATCC 700651 / DSM 11573). OC Bacteria; Proteobacteria; Gammaproteobacteria; Oceanospirillales; OC Alcanivoracaceae; Alcanivorax. OX NCBI_TaxID=393595; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16878126; DOI=10.1038/nbt1232; RA Schneiker S., Martins dos Santos V.A.P., Bartels D., Bekel T., RA Brecht M., Buhrmester J., Chernikova T.N., Denaro R., Ferrer M., RA Gertler C., Goesmann A., Golyshina O.V., Kaminski F., Khachane A.N., RA Lang S., Linke B., McHardy A.C., Meyer F., Nechitaylo T., Puehler A., RA Regenhardt D., Rupp O., Sabirova J.S., Selbitschka W., Yakimov M.M., RA Timmis K.N., Vorhoelter F.-J., Weidner S., Kaiser O., Golyshin P.N.; RT "Genome sequence of the ubiquitous hydrocarbon-degrading marine RT bacterium Alcanivorax borkumensis."; RL Nat. Biotechnol. 24:997-1004(2006). CC -!- CATALYTIC ACTIVITY: ATP + 5-amino-1-(5-phospho-D- CC ribosyl)imidazole-4-carboxylate + L-aspartate = ADP + phosphate + CC (S)-2-(5-amino-1-(5-phospho-D-ribosyl)imidazole-4- CC carboxamido)succinate. CC -!- PATHWAY: Purine metabolism; IMP biosynthesis via de novo pathway; CC 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide from N(2)- CC formyl-N(1)-(5-phospho-D-ribosyl)glycinamide: step 4/5. CC -!- SIMILARITY: Belongs to the SAICAR synthetase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AM286690; CAL16227.1; -; Genomic_DNA. DR RefSeq; YP_692499.1; -. DR GeneID; 4211142; -. DR GenomeReviews; AM286690_GR; ABO_0779. DR KEGG; abo:ABO_0779; -. DR NMPDR; fig|393595.12.peg.783; -. DR HOGENOM; Q0VRH1; -. DR OMA; Q0VRH1; TAFNAQK. DR BioCyc; ABOR393595:ABO_0779-MON; -. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0004639; F:phosphoribosylaminoimidazolesuccinocarboxam...; IEA:HAMAP. DR GO; GO:0006164; P:purine nucleotide biosynthetic process; IEA:HAMAP. DR HAMAP; MF_00137; -; 1. DR InterPro; IPR013816; ATP_grasp_subdomain_2. DR InterPro; IPR001636; SAICAR_synt. DR InterPro; IPR018236; SAICAR_synthetase_CS. DR Gene3D; G3DSA:3.30.470.20; ATP_grasp_subdomain_2; 1. DR PANTHER; PTHR11609; SAICAR_synt; 1. DR Pfam; PF01259; SAICAR_synt; 1. DR ProDom; PD003043; SAICAR_synt; 1. DR TIGRFAMs; TIGR00081; purC; 1. DR PROSITE; PS01057; SAICAR_SYNTHETASE_1; 1. DR PROSITE; PS01058; SAICAR_SYNTHETASE_2; 1. PE 3: Inferred from homology; KW ATP-binding; Complete proteome; Ligase; Nucleotide-binding; KW Purine biosynthesis. FT CHAIN 1 238 Phosphoribosylaminoimidazole- FT succinocarboxamide synthase. FT /FTId=PRO_1000018661. SQ SEQUENCE 238 AA; 26843 MW; EF070B14282C02A4 CRC64; MEKRDELYAG KAKSVYTTDD EDMLIMLFRD DTSAFDGKKK EALARKGAVN NQFNAAIMEK LKAAGIPCHF EKTLSATESL VKKLDMIPVE CVVRNIAAGS ICRRLGVEEG LELTPPTFEF FLKDDDLGDP MVNDFHIRSF GWASDDQVAQ MKTLTFAVND VLKQLFLDGG MLLVDYKLEF GMFKGEVLLG DEFSPDGCRL WDKDSREKLD KDRFRQGLGG VVEAYEEVGK RLGMTFEY //